1y4i
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Crystal structure of Citrobacter Freundii L-methionine-lyase
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedL-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes gamma-elimination of L-methionine. The crystal structure of MGL from Citrobacter freundii has been determined at 1.9 A resolution. The spatial fold of the protein is similar to those of MGLs from Pseudomonas putida and Trichomonas vaginalis. The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops. Structure of Citrobacter freundii L-methionine gamma-lyase.,Mamaeva DV, Morozova EA, Nikulin AD, Revtovich SV, Nikonov SV, Garber MB, Demidkina TV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt, 6):546-9. Epub 2005 Jun 1. PMID:16511092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 06:52, 23 August 2023.